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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Death effector domain containing 2

Top mentioned proteins: DEDD, PrP, caspase-8, FLIP, FLIP
Papers on DEDD2
Identification and Testing of Novel CARP-1 Functional Mimetic Compounds as Inhibitors of Non-Small Cell Lung and Triple Negative Breast Cancers.
Rishi et al., In J Biomed Nanotechnol, Sep 2015
In conclusion, while stimulation of pro-apoptotic CARP-1 and DEDD2 expression and their binding underscore a novel mechanism of apoptosis transduction by CFM compounds, our proof-of-concept xenograft studies demonstrate therapeutic potential of CFM-4 for TNBC and NSCLC.
Tandem DEDs and CARDs suggest novel mechanisms of signaling complex assembly.
Tung et al., Tainan City, Taiwan. In Apoptosis, Feb 2015
There are seven DED-containing proteins in human, including FADD, c-FLIP, caspase-8, caspase-10, DEDD, DEDD2, and PEA-15.
Targeting HSF1 sensitizes cancer cells to HSP90 inhibition.
Zhou et al., Cambridge, United States. In Oncotarget, 2013
To understand the mechanism of the combinational effect, we identified that a HSF1-target gene DEDD2 is involved in attenuating the effect of HSP90 inhibitors.
Transcriptome profiling and genome-wide DNA binding define the differential role of fenretinide and all-trans RA in regulating the death and survival of human hepatocellular carcinoma Huh7 cells.
Wan et al., Sacramento, United States. In Biochem Pharmacol, 2013
However, fenretinide specifically induced Fas/TNF╬▒-mediated apoptosis by increasing the expression of pro-apoptotic genes i.e., DEDD2, CASP8, CASP4, and HSPA1A/B; whereas, ATRA induced the expression of BIRC3 and TNFAIP3, which inhibit apoptosis by interacting with TRAF2.
Death effector domain-containing proteins.
Ramos et al., Honolulu, United States. In Cell Mol Life Sci, 2009
The seven standard DED-containing proteins are fas associated death domain protein (FADD), Caspase-8 and 10, cellular FLICE-like inhibitory protein (c-FLIP), death effector domain containing DNA binding (DEDD), DEDD2 and phosphoprotein enriched in astrocytes 15-Kda (PEA-15).
DEDD and DEDD2 associate with caspase-8/10 and signal cell death.
Yang et al., Philadelphia, United States. In Oncogene, 2003
DEDD and DEDD2 may be important mediators for death receptors and that they may target caspases to the nucleus.
DEDD regulates degradation of intermediate filaments during apoptosis.
Peter et al., Chicago, United States. In J Cell Biol, 2002
Early in apoptosis, both cytosolic DEDD and its close homologue DEDD2 formed filaments that colocalized with and depended on K8/18 and active caspase-3.
Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC.
Alnemri et al., Philadelphia, United States. In Cell Death Differ, 2002
FLAME-3 forms nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC
Identification and characterization of DEDD2, a death effector domain-containing protein.
Reed et al., Los Angeles, United States. In J Biol Chem, 2002
A novel Death Effector Domain-containing protein was identified, DEDD2, which is closest in amino acid sequence homology to death effector domain-containing DNA-binding protein, DEDD.
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